ReviewApplied microbiology and biotechnology2014
Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.
Review in Applied microbiology and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 79 citations in OpenAlex.
- Human colostrum as a probiotic reservoir: a genomic insights into potential probiotic traits.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Genetically Modified Lactic Acid Bacteria in the EU Food Chain: Applications, Benefits, and Risk Assessment.International journal of molecular sciences · 2026Review
- Detection and identification of pathogens using agents targeting the bacterial cell wall.Folia microbiologica · 2026Review
- Article
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- Grapevine protein Src2 mediates plant disease resistance during Lasiodiplodia theobromae infection.Plant physiology · 2025Article
- Isolation and Characterization of aJournal of microbiology and biotechnology · 2025Article
- M cells targeted H. pylori antigen SAM-FAdE displayed on bacterium-like particles induce protective immunity.Journal of nanobiotechnology · 2025Article
- A novel bacterium-like particles platform displaying antigens by new anchoring proteins induces efficacious immune responses.Frontiers in microbiology · 2024Article
- Spatial organization and proteome of a dual-species cyanobacterial biofilm alter among NmSystems · 2023Article
- Bacterium-like particles derived from probiotics: progress, challenges and prospects.Frontiers in immunology · 2023Review
- Staphylococcus aureus cell wall maintenance - the multifaceted roles of peptidoglycan hydrolases in bacterial growth, fitness, and virulence.FEMS microbiology reviews · 2022Review
- A novel, non-GMO surface display in Limosilactobacillus fermentum mediated by cell surface hydrolase without anchor motif.BMC microbiology · 2022Article
- Armed to the Teeth-The Oral Mucosa Immunity System and Microbiota.International journal of molecular sciences · 2022Review
- A subtractive proteomics approach for the identification of immunodominantFrontiers in immunology · 2022Article
- Comparative Genomics ofFrontiers in microbiology · 2022Article
- Novel LysM motifs for antigen display on lactobacilli for mucosal immunization.Scientific reports · 2021Article
- Improved antimicrobial spectrum of the N-acetylmuramoyl-L-alanine amidase from Latilactobacillus sakei upon LysM domain deletion.World journal of microbiology & biotechnology · 2021Article
- Spatial regulation of protein A in Staphylococcus aureus.Molecular microbiology · 2021Article
- Protein A of Staphylococcus aureus strain NCTC8325 interacted with heparin.Archives of microbiology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly or repeatedly in a large number of proteins of prokaryotes and eukaryotes. Since the mid-1990s, domains containing one or more of these LysM sequences originating from different LysM-containing proteins have been examined for purely scientific reasons as well as for their possible use in various medical and industrial applications. These studies range from detecting localized binding of LysM-containing proteins onto bacteria to actual bacterial cell surface analysis. On a more applied level, the possibilities of employing the LysM domains for cell immobilization, for the display of peptides, proteins, or enzymes on (bacterial) surfaces as well as their utility in the development of novel vaccines have been scrutinized. To serve these purposes, the chimeric proteins containing one or more of the LysM sequences have been produced and isolated from various prokaryotic and eukaryotic expression hosts. This review gives a succinct overview of the characteristics of the LysM domain and of current developments in its application potential.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.